title: Mutational analysis and a structural model of methyl-directed restriction enzyme Mrr.
abstract: The Mrr protein of Escherichia coli K12 is a cryptic Type IV restriction endonuclease whose activity appears to be triggered by high pressure stress. In this report we used high pressure to isolate and analyze several Mrr mutants, and generated a new structural model of the Mrr protein. The activity of a number of spontaneous and strategically constructed Mrr mutants is discussed in the light of this model, providing a first insight into the structure-function relationships of the Mrr enzyme.
authors.affiliation: Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw, Ul. Ks. Trojdena 4, 02-109 Warsaw, Poland.
authors.forename: Jerzy
authors.initials: J
authors.lastname: Orlowski
authors.forename: Mehari Tesfazgi
authors.initials: MT
authors.lastname: Mebrhatu
authors.forename: Chris W
authors.initials: CW
authors.lastname: Michiels
authors.forename: Janusz M
authors.initials: JM
authors.lastname: Bujnicki
authors.forename: Abram
authors.initials: A
authors.lastname: Aertsen
mesh_terms: D000483:Alleles; D000595:Amino Acid Sequence; D004252:DNA Mutational Analysis; D004262:DNA Restriction Enzymes / Q000737:chemistry* / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011312:Pressure; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
chemical_list: D029968:Escherichia coli Proteins; D004262:DNA Restriction Enzymes; C070141:Mrr protein, E coli